ID E1QQN5_VULDI Unreviewed; 1129 AA.
AC E1QQN5;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000256|RuleBase:RU366072};
DE EC=1.8.-.- {ECO:0000256|RuleBase:RU366072};
GN OrderedLocusNames=Vdis_2279 {ECO:0000313|EMBL:ADN51647.1};
OS Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 /
OS IC-017).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=572478 {ECO:0000313|EMBL:ADN51647.1, ECO:0000313|Proteomes:UP000006681};
RN [1] {ECO:0000313|EMBL:ADN51647.1, ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX PubMed=21304741;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S.,
RA Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017).";
RL Stand. Genomic Sci. 3:117-125(2010).
RN [2] {ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX DOI=10.4056/sigs.1113067;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y., Jeffries C., Rohde M., Spring S., Goker M.,
RA Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA Klenk H., Kyrpides N.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017T).";
RL Stand. Genomic Sci. 3:117-125(2010).
CC -!- FUNCTION: Part of a complex that catalyzes the reversible reduction of
CC CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB
CC (coenzyme B). {ECO:0000256|RuleBase:RU366072}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU366072};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|RuleBase:RU366072};
CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide
CC reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B
CC heterodisulfide: step 1/1. {ECO:0000256|RuleBase:RU366072}.
CC -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is composed
CC of three subunits; HdrA, HdrB and HdrC.
CC {ECO:0000256|RuleBase:RU366072}.
CC -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000256|ARBA:ARBA00006561,
CC ECO:0000256|RuleBase:RU366072}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002100; ADN51647.1; -; Genomic_DNA.
DR RefSeq; WP_013337372.1; NC_014537.1.
DR AlphaFoldDB; E1QQN5; -.
DR STRING; 572478.Vdis_2279; -.
DR GeneID; 9753234; -.
DR KEGG; vdi:Vdis_2279; -.
DR eggNOG; arCOG02235; Archaea.
DR eggNOG; arCOG02236; Archaea.
DR HOGENOM; CLU_004231_2_0_2; -.
DR OrthoDB; 32867at2157; -.
DR Proteomes; UP000006681; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.20; -; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 4.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR039650; HdrA-like.
DR InterPro; IPR003813; MvhD/FlpD.
DR PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR Pfam; PF14697; Fer4_21; 1.
DR Pfam; PF12800; Fer4_4; 1.
DR Pfam; PF02662; FlpD; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 3.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU366072};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU366072};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366072}; Iron {ECO:0000256|RuleBase:RU366072};
KW Iron-sulfur {ECO:0000256|RuleBase:RU366072};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366072};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366072};
KW Reference proteome {ECO:0000313|Proteomes:UP000006681}.
FT DOMAIN 96..126
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 912..941
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 942..971
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1129 AA; 123645 MW; 3C054272452E0A38 CRC64;
MPTNRILILG GGIAGIEAAL ALANMGYRVT LVEKSPAIGG KMAMLDKTFP TLDCSICIEG
PLISDVARHP YIELLAPAEL LDLTGSPGDF KARILVKPRY VTDDCTKCGQ CEDVCPVIVP
SEFEAGIGAR KAIYLPFPQA EPGIYMLDID HCLNKPPNYF PCDRCAKACD RNAIIYTMMP
KVIERDVAAV IVSTGFDLEK GDILGEYGYG RYMDVVTSLE FERLVNASGP SSGVVIKPST
GEEPENILLV SCVGSRNNRY NDYCSGFCCT YLLKQGIYAK VLHGIKNVTI MYMNDVRTYG
KGFESFFDRA LKEGINIVWG RPEVLGERNG KIVVRFEDTR NKKVVVNEYD MVVLAPSVKP
VGDMNKLSKI LNISLNRVGF VKTDPANPTL TTRPGIFVAG SASGPRDISE SVVTGLAAAV
QAIRYASPGV IEEEKYEETI EPYPIRVGVF VCHCGTNIAG VADVPALVEA AKQMPDVVHA
EDLQFACAKS SLDRITQVIK EKKLNRVVVA SCSPVTHLRF FQDSARRAGL NPYLVEMTNI
RNLDTWVHND RKVATEKAKD MIKMAVAKVH HMVPLQTIKL PVIKRALVIG CGPAGLAAAT
GLAGAGIETI LVEKSNECGG MLRRLNRLEP EGIEARKLLD RMVEEAKEVG VKFMLGTTIK
DVSGFTGNFH VILSNGVELD VGAIIVATGA KPYVPTEFNY GKDPRVLTTL DLENGKTVEG
KNVAIINCVG SRTSGRGCSR YCCAVGLSKA IELKSQGKNV VLIYRDIMGV NPEVEDLYKK
ARDAGVLFIR IPRKAELTEA IRMDTNKLIV HDVELGDDVE VPFDNIILNI GLVPSEDTDE
TSKILRLSKD QEGFLMEAHP KLGPVDTMTP GIFIAGAARG PKNVAEAIAE GYAAASRALM
MLAQGYVTKE PFIPKFDWSK CTKCGLCIKA CPYGAIRGVP GKWIEHIPAA CQGCGACVAE
CPQDAITLDA MSDDVILAQV EAALAEEPEK KVIMFTCAYC SYWAADNAGI FKMQYPPYAR
IIRLQCSSRL AWKHVKRAFE LGAAGVFVTG CRLGDCHYIT ANYNTVRRFE NWKKRLKNIG
VRDERFQLRL FGAPDVVDLV EAMKEAERVV KSVTKEEIEM TKQRIKQLR
//
